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The matrix (M) proteins of rhabdoviruses are multifunctional proteins essential for virus maturation and budding that also regulate the expression of viral and host proteins. We have solved the structures of M from the vesicular stomatitis virus serotype New Jersey (genus: Vesiculovirus) and from Lagos bat virus (genus: Lyssavirus), revealing that both share a common fold despite sharing no identifiable sequence homology. Strikingly, in both structures a stretch of residues from the otherwise-disordered N terminus of a crystallographically adjacent molecule is observed binding to a hydrophobic cavity on the surface of the protein, thereby forming non-covalent linear polymers of M in the crystals. While the overall topology of the interaction is conserved between the two structures, the molecular details of the interactions are completely different. The observed interactions provide a compelling model for the flexible self-assembly of the matrix protein during virion morphogenesis and may also modulate interactions with host proteins.

Original publication

DOI

10.1371/journal.ppat.1000251

Type

Journal article

Journal

PLoS Pathog

Publication Date

12/2008

Volume

4

Keywords

Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Multimerization, Protein Structure, Tertiary, Rhabdoviridae, Sequence Homology, Amino Acid, Serotyping, Vesicular stomatitis New Jersey virus, Viral Matrix Proteins, Virus Assembly